Manganese in PDB 6buu: Crystal Structure of AKT1 (Aa 144-480) with A Bisubstrate

All present enzymatic activity of Crystal Structure of AKT1 (Aa 144-480) with A Bisubstrate:
2.7.11.1;

The structure of Crystal Structure of AKT1 (Aa 144-480) with A Bisubstrate, PDB code: 6buu was solved by N.Chu, S.B.Gabelli, P.A.Cole, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.00 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	86.628, 56.267, 91.837, 90.00, 105.10, 90.00
R / Rfree (%)	18.3 / 23

The binding sites of Manganese atom in the Crystal Structure of AKT1 (Aa 144-480) with A Bisubstrate (pdb code 6buu). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of AKT1 (Aa 144-480) with A Bisubstrate, PDB code: 6buu:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of AKT1 (Aa 144-480) with A Bisubstrate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of AKT1 (Aa 144-480) with A Bisubstrate within 5.0Å range: probe atom residue distance (Å) B Occ F:Mn501 b:90.4 occ:1.00 OD2 A:ASP292 2.2 61.7 1.0 O2B F:ZXW7 2.5 65.4 1.0 O3A F:ZXW7 2.7 71.2 1.0 CG A:ASP292 2.9 51.0 1.0 PB F:ZXW7 2.9 74.5 1.0 OD1 A:ASP292 3.0 60.4 1.0 O1B F:ZXW7 3.3 75.1 1.0 OD1 A:ASN279 3.7 22.9 1.0 O F:HOH601 3.7 30.0 1.0 PA F:ZXW7 4.0 59.3 1.0 O5' F:ZXW7 4.2 56.0 1.0 CB A:ASP292 4.3 38.2 1.0 O3B F:ZXW7 4.3 70.7 1.0 C3' F:ZXW7 4.4 46.1 1.0 O1A F:ZXW7 4.5 69.9 1.0 C32 F:ZXW7 4.7 56.4 1.0 CG A:ASN279 4.8 21.7 1.0 O3G F:ZXW7 4.9 36.6 1.0 C2' F:ZXW7 4.9 40.3 1.0 C5' F:ZXW7 5.0 49.8 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of AKT1 (Aa 144-480) with A Bisubstrate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of AKT1 (Aa 144-480) with A Bisubstrate within 5.0Å range: probe atom residue distance (Å) B Occ G:Mn501 b:74.7 occ:1.00 O2B G:ZXW7 1.7 69.6 1.0 OD2 B:ASP292 2.3 30.0 1.0 PB G:ZXW7 2.8 59.5 1.0 OD1 B:ASP292 2.9 30.0 1.0 CG B:ASP292 3.0 30.0 1.0 O3A G:ZXW7 3.1 72.1 1.0 O1B G:ZXW7 3.2 50.0 1.0 OD1 B:ASN279 3.5 27.3 1.0 O B:HOH600 3.7 40.4 1.0 O G:HOH601 3.7 34.0 1.0 C5' G:ZXW7 4.0 58.7 1.0 S2G G:ZXW7 4.2 75.5 1.0 O3B G:ZXW7 4.3 61.0 1.0 PA G:ZXW7 4.4 68.4 1.0 CB B:ASP292 4.4 30.0 1.0 O5' G:ZXW7 4.5 59.3 1.0 C32 G:ZXW7 4.6 63.4 1.0 CG B:ASN279 4.7 21.4 1.0 NH1 G:ARG4 4.8 32.9 1.0 C3' G:ZXW7 4.8 50.1 1.0 O1A G:ZXW7 4.9 72.3 1.0 PG G:ZXW7 5.0 77.6 1.0

N.Chu, A.L.Salguero, A.Z.Liu, Z.Chen, D.R.Dempsey, S.B.Ficarro, W.M.Alexander, J.A.Marto, Y.Li, L.M.Amzel, S.B.Gabelli, P.A.Cole. Akt Kinase Activation Mechanisms Revealed Using Protein Semisynthesis. Cell V. 174 897 2018.
ISSN: ISSN 1097-4172
PubMed: 30078705
DOI: 10.1016/J.CELL.2018.07.003